P70478 · APC_RAT
- ProteinAdenomatous polyposis coli protein
- GeneApc
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids2842 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Tumor suppressor. Promotes rapid degradation of CTNNB1 and participates in Wnt signaling as a negative regulator. APC activity is correlated with its phosphorylation state. Activates the GEF activity of SPATA13 and ARHGEF4. Plays a role in hepatocyte growth factor (HGF)-induced cell migration (By similarity).
Required for MMP9 up-regulation via the JNK signaling pathway in colorectal tumor cells (By similarity).
Associates with both microtubules and actin filaments, components of the cytoskeleton (By similarity).
Plays a role in mediating the organization of F-actin into ordered bundles (By similarity).
Functions downstream of Rho GTPases and DIAPH1 to selectively stabilize microtubules (By similarity).
Acts as a mediator of ERBB2-dependent stabilization of microtubules at the cell cortex. It is required for the localization of MACF1 to the cell membrane and this localization of MACF1 is critical for its function in microtubule stabilization (By similarity).
Required for MMP9 up-regulation via the JNK signaling pathway in colorectal tumor cells (By similarity).
Associates with both microtubules and actin filaments, components of the cytoskeleton (By similarity).
Plays a role in mediating the organization of F-actin into ordered bundles (By similarity).
Functions downstream of Rho GTPases and DIAPH1 to selectively stabilize microtubules (By similarity).
Acts as a mediator of ERBB2-dependent stabilization of microtubules at the cell cortex. It is required for the localization of MACF1 to the cell membrane and this localization of MACF1 is critical for its function in microtubule stabilization (By similarity).
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Keywords
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameAdenomatous polyposis coli protein
- Short namesProtein APC
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Rattus
Accessions
- Primary accessionP70478
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: Associated with the microtubule network at the growing distal tip of microtubules. MAPRE1 may be required for targeting to the growing microtubule plus ends. Accumulates in the lamellipodium and ruffle membrane in response to hepatocyte growth factor (HGF) treatment. The MEMO1-RHOA-DIAPH1 signaling pathway controls localization of the phosphorylated form to the cell membrane.
Keywords
- Cellular component
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 523 | In an IQ-induced colon tumor. | ||||
Sequence: C → R |
Keywords
- Disease
PTM/Processing
Features
Showing features for initiator methionine, modified residue, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Initiator methionine | 1 | Removed | ||||
Sequence: M | ||||||
Modified residue | 2 | N-acetylalanine | ||||
Sequence: A | ||||||
Chain | PRO_0000064629 | 2-2842 | Adenomatous polyposis coli protein | |||
Sequence: AAASYDQLLKQVEALKMENSNLRQELEDNSNHLTELETEASNMKEVLKQLQGSIEDETMTSGQIDLLERLKEFNLDSNFPGVKLRSKMSLRSYGSREGSVSSRSGECSPVPMGSFPRRAFVNGSRESTGYLEELEKERSLLLADLDKEEKEKDWYYAQLQNLTKRIDSLPLTENFSLQTDMTRRQLEYEARQIRAAMEEQLGTCQDMEKRAQRRIARIQQIEKDILRVRQLLQSQAAEAERSSQSKHETASHEAERQLEGQGVAESNLATSGSGQSSAARVDHETAGVLSSSGTHSAPRRLTSHLGTKVEMVYSLLSMLGTHDKDDMSRTLLAMSSSQDSCISMRQSGCLPLLIQLLHGNDKDSVLLGNSRGSKEARARASAALHNIIHSQPDDKRGRREIRVLHLLEQIRAYCETCWEWQEAHEQGMDQDKNPMPAPVEHQICPAVCVLMKLSFDEEHRHAMNELGGLQAIAELLQVDCEMHGLTDDHYSVTLRRYAGMALTNLTFGDVANKATLCSMKGCMRALVAQLKSESEDLQQVIASVLRNLSWRADVNSKKTLREVGSVKALMECALEVKKESTLKSVLSALWNLSAHCTENKADICAVDGALAFLVGTLTYRSQTNTLAIIESGGGILRNVSSLIATNEDHRQILRENNCLQTLLQHLKSHSLTIVSNACGTLWNLSARNPKDQEALWDMGAVSMLKNLIHSKHKMIAMGSAAALRNLMANRPAKYKDANIMSPGSSLPSLHVRKQKALEAELDAQHLSETFDNIDNLSPKASHRSKQRHKQNLYGDYVFDASRHDDNRSDNFNTGNMTVLSPYLNTTVLPSSSSSRGSLDSSRSEKDRSLERERGIGLSTYHSATENPGTSSKRGLQLSATAAQIAKVMEEVSALHTSQDDRSPASAAELHCVAEERTAARRSSASHTHPNTHNFAKSESSNRTCSMPYAKVEYKRSSNDSLNSVTSSDGYGKRGQMKPSVESYSEDDEGKFCSYGQYPADLAHKIHSANHMDDNGGELDTPINYSLKYSDEQLNSGRQSPSQNERWARPKHVIEDEIKQNEQRQSRSQNTNFPVYSENTDDKHLKFQQHFGQQECVSPYRSRGTNGSETNRMGSSHAVNQNVNQSLCQEDDYEDDKPTNYSERYSEEEQHEEEERPTNYSIKYNEEKHHVDQPIDYSLKYATDISSSQKPSFSFSKTPSVQGTKTEHNSPSSEAASAPSSNAKRQSQLHPSSAQRNGQTPKGTACKVPSINQETMQTYCVEDTPICFSRCSSLSSLSSAEDEIGCDQTTQEADSANTLQIAEIKENDVTRSAQDPASDVPAVSQSTRTKPSRLQASGLASESARHKAVEFSSGAKSPSKSGAQTPKSPPEHYVQETPLVFSRCTSVSSLDSFESRSIASSVQSEPCSGMVSGIVSPSDLPDSPGQTMPPSRSKTPPPPPPPQPVQTKREVPKTKVPAAEQREGGPKQTAVSAAVQRVQVLPDADTLLHFATESTPDGFSCSSSLSALSLDEPFIQKDVELRIMPPVQENDNGNETEPEQPEESNENQDKEVEKPDSEKDLLDDSDDDDIEILEECIISAMPTKSSRKAKKLAQTASKLPPPVARKPSQLPVYKLLPSQSRLQAQKHVSFTPGDDVPRVYCVEGTPINFSTATSLSDLTIESPPNELAAGDGVRASVQSGEFEKRDTIPTEGRSTDEAQRGKVSSIAIPDLDGSKAEEGDILAECINSALPKGRSHKPFRVKKIMDQVQQASMTSSGTNKNQIDTKKKKPTSPVKPMPQNTEYRTRVRKNTDSKVNVNTEETFSDNKDSKKQSLKNNPKDLNDKLPDNEDRVRGGFTFDSPHHYAPIEGTPYCFSRNDSLSSLDFDDDDVDLSREKAELRKGKESKDSEAKVTCHTEPSSSQQSARKAQASTKHPVNRGPSKPLLQEQPTFPQSSKDVPDRGAATDEKLQNFAIENTPVCFSRNSSLSSLSDVDQENNNNEETGPVRDAEPANAQGQPGKPQASGYAPKSFHVEDTPVCFSRNSSLSSLSIDSEDDLLRECISSAMPKKRRPSRLKGEGEWQSPRKVGSVLAEDLTLDLKDIQRPESEHGLSPDSENFDWKAIQEGANSIVSSLHQAAAAAACLSRQASSDSDSILSLKSGVSLGSPFHLTPDQEEKPFTSHKGPRILKPGEKSTLEAKKIESENKGIKGGKKVYKSLITGKIRSNSEISSQMKQPLQTNMPSISRGRTMIHIPGVRNSSSSTSPVSKKGPPLKTPASKSPSEGPVATTSPRGTKPAVKSELSPITRQTSHISGSNKGPSRSGSRDSTPSRPTQQPLSRPMQSPGRNSISPGRNGISTPNKLSQLPRTSSPSTASTKSSGSGKMSYTSPGRQLSQQNLSKQTGLSKNASSIPRSESASKGLNQMNNSNGSNKKVELSRMSSTKSSGSESDRSERPALVRQSTFIKEAPSPTLRRKLEESASFESLSPSSRPDSPTRSQAQTPVLSPSLPDMSLSTHPSVQAGGWRKLPPNLSPTIEYSDGRPSKRHDIARSHSESPSRLPVNRAGTWKREHSKHSSSLPRVSTWRRTGSSSSILSASSESSEKAKSEDEKHVNSVPGPRQMKENQVPTKGTWRKIKESEISPTNTVSQTTSSGAASGAESKTLIYQMAPAVSRTEDVWVRIEDCPINNPRSGRSPTGNTPPVIDSISEKGNPSIKDSKDTQGKQSVGSGSPVQTVGLENRLNSFIQVEAPEQKGTETKAGQGSPAPVAETGETCMAERTPFSSSSSSKHSSPSGTVAARVTPFNYNPSPRKSSADSTSARPSQIPTPVGSSTKKRDSKTDSTESSGAQSPKRHSGSYLVTSV | ||||||
Modified residue | 105 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 109 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 742 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 746 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 778 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 906 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 985 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1036 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1040 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1357 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1368 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1382 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1389 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1392 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1435 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 1565 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1714 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1772 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1859 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1861 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1862 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1969 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1971 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 2087 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 2092 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 2125 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 2129 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 2130 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 2132 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 2151 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 2260 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 2270 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 2283 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 2473 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 2535 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 2569 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 2671 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 2674 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 2679 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 2710 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 2723 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 2788 | Phosphoserine | ||||
Sequence: S |
Post-translational modification
Phosphorylated; phosphorylation enhances the F-actin bundling activity (By similarity).
Phosphorylated by GSK3B
Phosphorylated by GSK3B
Ubiquitinated, leading to its degradation by the proteasome. Ubiquitination is facilitated by Axin. Deubiquitinated by ZRANB1/TRABID (By similarity).
Keywords
- PTM
Proteomic databases
PTM databases
Interaction
Subunit
Forms homooligomers (Probable). Found in a complex consisting of ARHGEF4, APC and CTNNB1 (By similarity).
Found in a complex composed of MACF1, APC, AXIN1, CTNNB1 and GSK3B (PubMed:16815997).
The complex composed, at least, of APC, CTNNB1 and GSK3B interacts with JPT1; the interaction requires the inactive form of GSK3B (phosphorylated at 'Ser-9') (By similarity).
Interacts with APC2 (By similarity).
Interacts with DLG1 (via PDZ domains) and DLG3 (via PDZ domains) (By similarity).
Interacts with alpha- and beta-catenins (By similarity).
Interacts with AXIN1 (via RGS domain) (By similarity).
Interacts with ARHGEF4 (via N-terminus) (By similarity).
Interacts (via C-terminal residues 2674-2843) with MAPRE1 (via C-terminal residues 206-211); the interaction inhibits association with and bundling of F-actin (By similarity).
Interacts with MAPRE2 and MAPRE3 (via C-terminus) (By similarity).
Interacts with DIAPH1; DIAPH1 acts as a scaffold protein for MAPRE1 and APC to stabilize microtubules and promote cell migration (By similarity).
Interacts with DIAPH2 (By similarity).
Interacts with SCRIB; may mediate APC targeting to adherens junctions of epithelial cells (By similarity).
Interacts with SPATA13 (via N-terminus and SH3 domain) (By similarity).
Interacts with ASAP1 (via SH3 domain) (By similarity).
Interacts (at the cell membrane) with AMER1 and AMER2 (via ARM repeats) (By similarity).
Interacts with KHDRBS1 (By similarity).
Interacts with actin; binds both to F-actin and actin filament bundles (By similarity).
Found in a complex composed of MACF1, APC, AXIN1, CTNNB1 and GSK3B (PubMed:16815997).
The complex composed, at least, of APC, CTNNB1 and GSK3B interacts with JPT1; the interaction requires the inactive form of GSK3B (phosphorylated at 'Ser-9') (By similarity).
Interacts with APC2 (By similarity).
Interacts with DLG1 (via PDZ domains) and DLG3 (via PDZ domains) (By similarity).
Interacts with alpha- and beta-catenins (By similarity).
Interacts with AXIN1 (via RGS domain) (By similarity).
Interacts with ARHGEF4 (via N-terminus) (By similarity).
Interacts (via C-terminal residues 2674-2843) with MAPRE1 (via C-terminal residues 206-211); the interaction inhibits association with and bundling of F-actin (By similarity).
Interacts with MAPRE2 and MAPRE3 (via C-terminus) (By similarity).
Interacts with DIAPH1; DIAPH1 acts as a scaffold protein for MAPRE1 and APC to stabilize microtubules and promote cell migration (By similarity).
Interacts with DIAPH2 (By similarity).
Interacts with SCRIB; may mediate APC targeting to adherens junctions of epithelial cells (By similarity).
Interacts with SPATA13 (via N-terminus and SH3 domain) (By similarity).
Interacts with ASAP1 (via SH3 domain) (By similarity).
Interacts (at the cell membrane) with AMER1 and AMER2 (via ARM repeats) (By similarity).
Interacts with KHDRBS1 (By similarity).
Interacts with actin; binds both to F-actin and actin filament bundles (By similarity).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | P70478 | Dlg4 P31016 | 2 | EBI-631663, EBI-375655 |
Protein-protein interaction databases
Family & Domains
Features
Showing features for coiled coil, region, compositional bias, repeat, motif.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Coiled coil | 2-62 | |||||
Sequence: AAASYDQLLKQVEALKMENSNLRQELEDNSNHLTELETEASNMKEVLKQLQGSIEDETMTS | ||||||
Coiled coil | 125-260 | |||||
Sequence: SRESTGYLEELEKERSLLLADLDKEEKEKDWYYAQLQNLTKRIDSLPLTENFSLQTDMTRRQLEYEARQIRAAMEEQLGTCQDMEKRAQRRIARIQQIEKDILRVRQLLQSQAAEAERSSQSKHETASHEAERQLE | ||||||
Region | 238-304 | Disordered | ||||
Sequence: AEAERSSQSKHETASHEAERQLEGQGVAESNLATSGSGQSSAARVDHETAGVLSSSGTHSAPRRLTS | ||||||
Compositional bias | 242-260 | Basic and acidic residues | ||||
Sequence: RSSQSKHETASHEAERQLE | ||||||
Compositional bias | 264-281 | Polar residues | ||||
Sequence: VAESNLATSGSGQSSAAR | ||||||
Compositional bias | 288-302 | Polar residues | ||||
Sequence: GVLSSSGTHSAPRRL | ||||||
Repeat | 451-493 | ARM 1 | ||||
Sequence: LMKLSFDEEHRHAMNELGGLQAIAELLQVDCEMHGLTDDHYSV | ||||||
Repeat | 503-545 | ARM 2 | ||||
Sequence: LTNLTFGDVANKATLCSMKGCMRALVAQLKSESEDLQQVIASV | ||||||
Repeat | 546-589 | ARM 3 | ||||
Sequence: LRNLSWRADVNSKKTLREVGSVKALMECALEVKKESTLKSVLSA | ||||||
Repeat | 590-636 | ARM 4 | ||||
Sequence: LWNLSAHCTENKADICAVDGALAFLVGTLTYRSQTNTLAIIESGGGI | ||||||
Repeat | 637-681 | ARM 5 | ||||
Sequence: LRNVSSLIATNEDHRQILRENNCLQTLLQHLKSHSLTIVSNACGT | ||||||
Repeat | 682-723 | ARM 6 | ||||
Sequence: LWNLSARNPKDQEALWDMGAVSMLKNLIHSKHKMIAMGSAAA | ||||||
Repeat | 724-765 | ARM 7 | ||||
Sequence: LRNLMANRPAKYKDANIMSPGSSLPSLHVRKQKALEAELDAQ | ||||||
Region | 828-877 | Disordered | ||||
Sequence: VLPSSSSSRGSLDSSRSEKDRSLERERGIGLSTYHSATENPGTSSKRGLQ | ||||||
Compositional bias | 840-855 | Basic and acidic residues | ||||
Sequence: DSSRSEKDRSLERERG | ||||||
Compositional bias | 860-877 | Polar residues | ||||
Sequence: TYHSATENPGTSSKRGLQ | ||||||
Region | 921-942 | Disordered | ||||
Sequence: RRSSASHTHPNTHNFAKSESSN | ||||||
Compositional bias | 924-942 | Polar residues | ||||
Sequence: SASHTHPNTHNFAKSESSN | ||||||
Compositional bias | 956-973 | Polar residues | ||||
Sequence: RSSNDSLNSVTSSDGYGK | ||||||
Region | 956-988 | Disordered | ||||
Sequence: RSSNDSLNSVTSSDGYGKRGQMKPSVESYSEDD | ||||||
Region | 1018-1167 | Interaction with catenins | ||||
Sequence: ELDTPINYSLKYSDEQLNSGRQSPSQNERWARPKHVIEDEIKQNEQRQSRSQNTNFPVYSENTDDKHLKFQQHFGQQECVSPYRSRGTNGSETNRMGSSHAVNQNVNQSLCQEDDYEDDKPTNYSERYSEEEQHEEEERPTNYSIKYNEE | ||||||
Region | 1058-1078 | Disordered | ||||
Sequence: IKQNEQRQSRSQNTNFPVYSE | ||||||
Compositional bias | 1064-1078 | Polar residues | ||||
Sequence: RQSRSQNTNFPVYSE | ||||||
Compositional bias | 1092-1128 | Polar residues | ||||
Sequence: GQQECVSPYRSRGTNGSETNRMGSSHAVNQNVNQSLC | ||||||
Region | 1092-1166 | Disordered | ||||
Sequence: GQQECVSPYRSRGTNGSETNRMGSSHAVNQNVNQSLCQEDDYEDDKPTNYSERYSEEEQHEEEERPTNYSIKYNE | ||||||
Compositional bias | 1130-1166 | Basic and acidic residues | ||||
Sequence: EDDYEDDKPTNYSERYSEEEQHEEEERPTNYSIKYNE | ||||||
Region | 1188-1249 | Disordered | ||||
Sequence: SQKPSFSFSKTPSVQGTKTEHNSPSSEAASAPSSNAKRQSQLHPSSAQRNGQTPKGTACKVP | ||||||
Compositional bias | 1306-1339 | Polar residues | ||||
Sequence: ENDVTRSAQDPASDVPAVSQSTRTKPSRLQASGL | ||||||
Region | 1306-1373 | Disordered | ||||
Sequence: ENDVTRSAQDPASDVPAVSQSTRTKPSRLQASGLASESARHKAVEFSSGAKSPSKSGAQTPKSPPEHY | ||||||
Compositional bias | 1354-1371 | Polar residues | ||||
Sequence: GAKSPSKSGAQTPKSPPE | ||||||
Region | 1398-1474 | Disordered | ||||
Sequence: IASSVQSEPCSGMVSGIVSPSDLPDSPGQTMPPSRSKTPPPPPPPQPVQTKREVPKTKVPAAEQREGGPKQTAVSAA | ||||||
Compositional bias | 1430-1447 | Pro residues | ||||
Sequence: PSRSKTPPPPPPPQPVQT | ||||||
Region | 1525-1568 | Disordered | ||||
Sequence: PPVQENDNGNETEPEQPEESNENQDKEVEKPDSEKDLLDDSDDD | ||||||
Compositional bias | 1543-1559 | Basic and acidic residues | ||||
Sequence: ESNENQDKEVEKPDSEK | ||||||
Region | 1584-1609 | Disordered | ||||
Sequence: KSSRKAKKLAQTASKLPPPVARKPSQ | ||||||
Region | 1661-1711 | Disordered | ||||
Sequence: ESPPNELAAGDGVRASVQSGEFEKRDTIPTEGRSTDEAQRGKVSSIAIPDL | ||||||
Compositional bias | 1678-1698 | Basic and acidic residues | ||||
Sequence: QSGEFEKRDTIPTEGRSTDEA | ||||||
Region | 1748-1950 | Disordered | ||||
Sequence: VQQASMTSSGTNKNQIDTKKKKPTSPVKPMPQNTEYRTRVRKNTDSKVNVNTEETFSDNKDSKKQSLKNNPKDLNDKLPDNEDRVRGGFTFDSPHHYAPIEGTPYCFSRNDSLSSLDFDDDDVDLSREKAELRKGKESKDSEAKVTCHTEPSSSQQSARKAQASTKHPVNRGPSKPLLQEQPTFPQSSKDVPDRGAATDEKLQ | ||||||
Compositional bias | 1785-1837 | Basic and acidic residues | ||||
Sequence: TRVRKNTDSKVNVNTEETFSDNKDSKKQSLKNNPKDLNDKLPDNEDRVRGGFT | ||||||
Compositional bias | 1861-1893 | Basic and acidic residues | ||||
Sequence: SSLDFDDDDVDLSREKAELRKGKESKDSEAKVT | ||||||
Region | 1864-1891 | Highly charged | ||||
Sequence: DFDDDDVDLSREKAELRKGKESKDSEAK | ||||||
Compositional bias | 1894-1916 | Polar residues | ||||
Sequence: CHTEPSSSQQSARKAQASTKHPV | ||||||
Compositional bias | 1963-1984 | Polar residues | ||||
Sequence: RNSSLSSLSDVDQENNNNEETG | ||||||
Region | 1963-2010 | Disordered | ||||
Sequence: RNSSLSSLSDVDQENNNNEETGPVRDAEPANAQGQPGKPQASGYAPKS | ||||||
Region | 2034-2058 | Interaction with AXIN1 | ||||
Sequence: EDDLLRECISSAMPKKRRPSRLKGE | ||||||
Compositional bias | 2043-2061 | Basic and acidic residues | ||||
Sequence: SSAMPKKRRPSRLKGEGEW | ||||||
Region | 2043-2067 | Disordered | ||||
Sequence: SSAMPKKRRPSRLKGEGEWQSPRKV | ||||||
Region | 2148-2173 | Disordered | ||||
Sequence: FHLTPDQEEKPFTSHKGPRILKPGEK | ||||||
Compositional bias | 2155-2173 | Basic and acidic residues | ||||
Sequence: EEKPFTSHKGPRILKPGEK | ||||||
Region | 2167-2674 | Basic region | ||||
Sequence: ILKPGEKSTLEAKKIESENKGIKGGKKVYKSLITGKIRSNSEISSQMKQPLQTNMPSISRGRTMIHIPGVRNSSSSTSPVSKKGPPLKTPASKSPSEGPVATTSPRGTKPAVKSELSPITRQTSHISGSNKGPSRSGSRDSTPSRPTQQPLSRPMQSPGRNSISPGRNGISTPNKLSQLPRTSSPSTASTKSSGSGKMSYTSPGRQLSQQNLSKQTGLSKNASSIPRSESASKGLNQMNNSNGSNKKVELSRMSSTKSSGSESDRSERPALVRQSTFIKEAPSPTLRRKLEESASFESLSPSSRPDSPTRSQAQTPVLSPSLPDMSLSTHPSVQAGGWRKLPPNLSPTIEYSDGRPSKRHDIARSHSESPSRLPVNRAGTWKREHSKHSSSLPRVSTWRRTGSSSSILSASSESSEKAKSEDEKHVNSVPGPRQMKENQVPTKGTWRKIKESEISPTNTVSQTTSSGAASGAESKTLIYQMAPAVSRTEDVWVRIEDCPINNPRSGRS | ||||||
Compositional bias | 2234-2249 | Polar residues | ||||
Sequence: PGVRNSSSSTSPVSKK | ||||||
Region | 2234-2641 | Disordered | ||||
Sequence: PGVRNSSSSTSPVSKKGPPLKTPASKSPSEGPVATTSPRGTKPAVKSELSPITRQTSHISGSNKGPSRSGSRDSTPSRPTQQPLSRPMQSPGRNSISPGRNGISTPNKLSQLPRTSSPSTASTKSSGSGKMSYTSPGRQLSQQNLSKQTGLSKNASSIPRSESASKGLNQMNNSNGSNKKVELSRMSSTKSSGSESDRSERPALVRQSTFIKEAPSPTLRRKLEESASFESLSPSSRPDSPTRSQAQTPVLSPSLPDMSLSTHPSVQAGGWRKLPPNLSPTIEYSDGRPSKRHDIARSHSESPSRLPVNRAGTWKREHSKHSSSLPRVSTWRRTGSSSSILSASSESSEKAKSEDEKHVNSVPGPRQMKENQVPTKGTWRKIKESEISPTNTVSQTTSSGAASGAESK | ||||||
Compositional bias | 2261-2426 | Polar residues | ||||
Sequence: PSEGPVATTSPRGTKPAVKSELSPITRQTSHISGSNKGPSRSGSRDSTPSRPTQQPLSRPMQSPGRNSISPGRNGISTPNKLSQLPRTSSPSTASTKSSGSGKMSYTSPGRQLSQQNLSKQTGLSKNASSIPRSESASKGLNQMNNSNGSNKKVELSRMSSTKSSG | ||||||
Compositional bias | 2461-2499 | Polar residues | ||||
Sequence: SFESLSPSSRPDSPTRSQAQTPVLSPSLPDMSLSTHPSV | ||||||
Region | 2475-2842 | Interaction with DLG1 | ||||
Sequence: TRSQAQTPVLSPSLPDMSLSTHPSVQAGGWRKLPPNLSPTIEYSDGRPSKRHDIARSHSESPSRLPVNRAGTWKREHSKHSSSLPRVSTWRRTGSSSSILSASSESSEKAKSEDEKHVNSVPGPRQMKENQVPTKGTWRKIKESEISPTNTVSQTTSSGAASGAESKTLIYQMAPAVSRTEDVWVRIEDCPINNPRSGRSPTGNTPPVIDSISEKGNPSIKDSKDTQGKQSVGSGSPVQTVGLENRLNSFIQVEAPEQKGTETKAGQGSPAPVAETGETCMAERTPFSSSSSSKHSSPSGTVAARVTPFNYNPSPRKSSADSTSARPSQIPTPVGSSTKKRDSKTDSTESSGAQSPKRHSGSYLVTSV | ||||||
Compositional bias | 2519-2533 | Basic and acidic residues | ||||
Sequence: DGRPSKRHDIARSHS | ||||||
Compositional bias | 2557-2580 | Polar residues | ||||
Sequence: SLPRVSTWRRTGSSSSILSASSES | ||||||
Compositional bias | 2581-2596 | Basic and acidic residues | ||||
Sequence: SEKAKSEDEKHVNSVP | ||||||
Compositional bias | 2617-2639 | Polar residues | ||||
Sequence: ESEISPTNTVSQTTSSGAASGAE | ||||||
Region | 2664-2842 | Disordered | ||||
Sequence: CPINNPRSGRSPTGNTPPVIDSISEKGNPSIKDSKDTQGKQSVGSGSPVQTVGLENRLNSFIQVEAPEQKGTETKAGQGSPAPVAETGETCMAERTPFSSSSSSKHSSPSGTVAARVTPFNYNPSPRKSSADSTSARPSQIPTPVGSSTKKRDSKTDSTESSGAQSPKRHSGSYLVTSV | ||||||
Compositional bias | 2669-2686 | Polar residues | ||||
Sequence: PRSGRSPTGNTPPVIDSI | ||||||
Region | 2674-2842 | Interaction with MAPRE1 | ||||
Sequence: SPTGNTPPVIDSISEKGNPSIKDSKDTQGKQSVGSGSPVQTVGLENRLNSFIQVEAPEQKGTETKAGQGSPAPVAETGETCMAERTPFSSSSSSKHSSPSGTVAARVTPFNYNPSPRKSSADSTSARPSQIPTPVGSSTKKRDSKTDSTESSGAQSPKRHSGSYLVTSV | ||||||
Compositional bias | 2697-2730 | Polar residues | ||||
Sequence: SKDTQGKQSVGSGSPVQTVGLENRLNSFIQVEAP | ||||||
Compositional bias | 2756-2812 | Polar residues | ||||
Sequence: AERTPFSSSSSSKHSSPSGTVAARVTPFNYNPSPRKSSADSTSARPSQIPTPVGSST | ||||||
Motif | 2802-2805 | Microtubule tip localization signal | ||||
Sequence: SQIP | ||||||
Compositional bias | 2822-2842 | Polar residues | ||||
Sequence: TESSGAQSPKRHSGSYLVTSV | ||||||
Motif | 2840-2842 | PDZ-binding | ||||
Sequence: TSV |
Domain
The microtubule tip localization signal (MtLS) motif; mediates interaction with MAPRE1 and targeting to the growing microtubule plus ends.
The basic region (residues 2167-2674) mediates the association with both microtubule and actin proteins and promotes the bundling of F-actin.
Sequence similarities
Belongs to the adenomatous polyposis coli (APC) family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length2,842
- Mass (Da)310,533
- Last updated1997-02-01 v1
- Checksum3CBB2EA8A34E8F47
Computationally mapped potential isoform sequences
There are 3 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A0G2K8G0 | A0A0G2K8G0_RAT | Apc | 2860 | ||
G3V8Q9 | G3V8Q9_RAT | Apc | 2842 | ||
A0A8I5ZR24 | A0A8I5ZR24_RAT | Apc | 2825 |
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 242-260 | Basic and acidic residues | ||||
Sequence: RSSQSKHETASHEAERQLE | ||||||
Compositional bias | 264-281 | Polar residues | ||||
Sequence: VAESNLATSGSGQSSAAR | ||||||
Compositional bias | 288-302 | Polar residues | ||||
Sequence: GVLSSSGTHSAPRRL | ||||||
Compositional bias | 840-855 | Basic and acidic residues | ||||
Sequence: DSSRSEKDRSLERERG | ||||||
Compositional bias | 860-877 | Polar residues | ||||
Sequence: TYHSATENPGTSSKRGLQ | ||||||
Compositional bias | 924-942 | Polar residues | ||||
Sequence: SASHTHPNTHNFAKSESSN | ||||||
Compositional bias | 956-973 | Polar residues | ||||
Sequence: RSSNDSLNSVTSSDGYGK | ||||||
Compositional bias | 1064-1078 | Polar residues | ||||
Sequence: RQSRSQNTNFPVYSE | ||||||
Compositional bias | 1092-1128 | Polar residues | ||||
Sequence: GQQECVSPYRSRGTNGSETNRMGSSHAVNQNVNQSLC | ||||||
Compositional bias | 1130-1166 | Basic and acidic residues | ||||
Sequence: EDDYEDDKPTNYSERYSEEEQHEEEERPTNYSIKYNE | ||||||
Compositional bias | 1306-1339 | Polar residues | ||||
Sequence: ENDVTRSAQDPASDVPAVSQSTRTKPSRLQASGL | ||||||
Compositional bias | 1354-1371 | Polar residues | ||||
Sequence: GAKSPSKSGAQTPKSPPE | ||||||
Compositional bias | 1430-1447 | Pro residues | ||||
Sequence: PSRSKTPPPPPPPQPVQT | ||||||
Compositional bias | 1543-1559 | Basic and acidic residues | ||||
Sequence: ESNENQDKEVEKPDSEK | ||||||
Compositional bias | 1678-1698 | Basic and acidic residues | ||||
Sequence: QSGEFEKRDTIPTEGRSTDEA | ||||||
Compositional bias | 1785-1837 | Basic and acidic residues | ||||
Sequence: TRVRKNTDSKVNVNTEETFSDNKDSKKQSLKNNPKDLNDKLPDNEDRVRGGFT | ||||||
Compositional bias | 1861-1893 | Basic and acidic residues | ||||
Sequence: SSLDFDDDDVDLSREKAELRKGKESKDSEAKVT | ||||||
Compositional bias | 1894-1916 | Polar residues | ||||
Sequence: CHTEPSSSQQSARKAQASTKHPV | ||||||
Compositional bias | 1963-1984 | Polar residues | ||||
Sequence: RNSSLSSLSDVDQENNNNEETG | ||||||
Compositional bias | 2043-2061 | Basic and acidic residues | ||||
Sequence: SSAMPKKRRPSRLKGEGEW | ||||||
Compositional bias | 2155-2173 | Basic and acidic residues | ||||
Sequence: EEKPFTSHKGPRILKPGEK | ||||||
Compositional bias | 2234-2249 | Polar residues | ||||
Sequence: PGVRNSSSSTSPVSKK | ||||||
Compositional bias | 2261-2426 | Polar residues | ||||
Sequence: PSEGPVATTSPRGTKPAVKSELSPITRQTSHISGSNKGPSRSGSRDSTPSRPTQQPLSRPMQSPGRNSISPGRNGISTPNKLSQLPRTSSPSTASTKSSGSGKMSYTSPGRQLSQQNLSKQTGLSKNASSIPRSESASKGLNQMNNSNGSNKKVELSRMSSTKSSG | ||||||
Compositional bias | 2461-2499 | Polar residues | ||||
Sequence: SFESLSPSSRPDSPTRSQAQTPVLSPSLPDMSLSTHPSV | ||||||
Compositional bias | 2519-2533 | Basic and acidic residues | ||||
Sequence: DGRPSKRHDIARSHS | ||||||
Compositional bias | 2557-2580 | Polar residues | ||||
Sequence: SLPRVSTWRRTGSSSSILSASSES | ||||||
Compositional bias | 2581-2596 | Basic and acidic residues | ||||
Sequence: SEKAKSEDEKHVNSVP | ||||||
Compositional bias | 2617-2639 | Polar residues | ||||
Sequence: ESEISPTNTVSQTTSSGAASGAE | ||||||
Compositional bias | 2669-2686 | Polar residues | ||||
Sequence: PRSGRSPTGNTPPVIDSI | ||||||
Compositional bias | 2697-2730 | Polar residues | ||||
Sequence: SKDTQGKQSVGSGSPVQTVGLENRLNSFIQVEAP | ||||||
Compositional bias | 2756-2812 | Polar residues | ||||
Sequence: AERTPFSSSSSSKHSSPSGTVAARVTPFNYNPSPRKSSADSTSARPSQIPTPVGSST | ||||||
Compositional bias | 2822-2842 | Polar residues | ||||
Sequence: TESSGAQSPKRHSGSYLVTSV |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
D38629 EMBL· GenBank· DDBJ | BAA07609.1 EMBL· GenBank· DDBJ | mRNA |